Influenza A H1N1 (A/California/04/2009) Neuraminidase / NA (Active) sinobiological 11058-VNAHC

$194.00
In stock
SKU
11058-VNAHC
Catalog No.SizePrice (USD)
11058-VNAHC-100100 U$201.43
11058-VNAHC-200200 U$343.62

General Information

FormulationLyophilized from sterile PBS, 0.6% Triton X-100, 7% Trehalose, 6% Mannitol, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet or the lot-specific COA.
EndotoxinPlease contact us for more information.
ShippingIn general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & StorageSamples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
ReconstitutionTo find reconstitution info, click on 'COA' at the top of the page, enter the lot number and product size for the lot-specific COA.
ActivityMeasured by its ability to cleave a fluorogenic substrate, 2’-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid. One unit is defined as the amount of enzyme required to cleave 1 nmole of 2'-(4-Methylumbelliferyl)-α-D-N-acetylneuraminic acid per minute at pH 7.5 at 37℃.
Protein ConstructionA DNA sequence encoding the Influenza A virus (A/California/04/2009 (H1N1)) neuraminidase (ACP41107.1) (His 36-Lys 469) was expressed, Collected cell lysates are validated for neuraminidase activity.
Accession#ACP41107.1
Expressed HostHEK293 Cells
SpeciesH1N1
Molecule MassThe recombinant influenza A H1N1 Neuraminidase comprises 434 amino acids and has a predicted molecular mass of 47.8 KDa.

Background Information

DescriptionNeuraminidases are enzymes that cleave sialic acid groups from glycoproteins. Influenza neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Influenza neuraminidase is composed of four identical subunits arranged in a square. It is normally attached to the virus surface through a long protein stalk. The active sites are in a deep depression on the upper surface. They bind to polysaccharide chains and clip off the sugars at the end. The surface of neuraminidase is decorated with several polysaccharide chains that are similar to the polysaccharide chains that decorate our cell surface proteins. Neuraminidase (NA) and hemagglutinin (HA) are major membrane glycoproteins found on the surface of the influenza virus. Hemagglutinin binds to the sialic acid-containing receptors on the surface of host cells during initial infection and at the end of an infectious cycle. Neuraminidase, on the other hand, cleaves the HA-sialic acid bondage from the newly formed virions and the host cell receptors during budding. Neuraminidase thus is described as a receptor-destroying enzyme that facilitates virus release and efficient spread of the progeny virus from cell to cell. Influenza antibody and influenza antibodies are very important research tools for influenza diagnosis, influenza vaccine development, and anti-influenza virus therapy development. The monoclonal or polyclonal antibody can be raised with protein based antigen or peptide-based antigen. Antibodies raised with protein-based antigen could have better specificity and/or binding affinity than antibodies raised with peptide based antigen, but the cost associated with the recombinant protein antigen is usually higher. Anti-influenza virus hemagglutinin (HA) monoclonal antibody or polyclonal antibody can be used for ELISA assay, western blotting detection, Immunohistochemistry (IHC), flow cytometry, neutralization assay, hemagglutinin inhibition assay, and early diagnosis of influenza viral infection. Sino Biological has developed state-of-the-art monoclonal antibody development technology platforms: mouse monoclonal antibody and rabbit monoclonal antibody. Our rabbit monoclonal antibody platform is one of a kind and offers some unique advantages over mouse monoclonal antibodies, such as high affinity, low cross-reactivity with rabbit polyclonal antibodies.
References
  1. Sardet C., et al. ,(1989), Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter. Cell 56:271-280.
  2. Sardet C., et al. , (1990), Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD.Science 247:723-726.
  3. Tse C.-M., et al. ,(1991), Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger.EMBO J. 10:1957-1967.

title: Discovery of Influenza Neuraminidase Inhibitors: Structure-Based Virtual Screening and Biological Evaluation of Novel Chemotypes.
authors: Rosaria Gitto; Lisa Lombardo; ...; Francesca Marino-Merlo
journal: Molecules (Basel, Switzerland)
date: 2025-12-11
pmid: 41375232
cited_by_count: 0
techniques: Activity Assay; Control; Fluorescence; Inhibition; Microplate Reader Absorbance Measurement; Positive Control; Recombinant; Sonication
bioz_score: 95

title: Lipoteichoic acid mediates binding of Streptococcus pneumoniae and influenza A virus.
authors: Trevor Penix; Jenna Favazza; ...; Hannah M Rowe
journal: mSphere
date: 2025-11-28
pmid: 41313015
cited_by_count: 0
techniques: Concentration Assay; Control; Incubation
bioz_score: 95

title: Vectored long-term co-delivery of antibodies for SARS-CoV-2, RSV and Influenza prophylaxis.
authors: Stine Sofie Frank Lende; Frederik Holm Rothemejer; ...; Martin Tolstrup
journal: Virology
date: 2025-07-31
pmid: 40413832
doi: 10.1016/j.virol.2025.110573
cited_by_count: 1
techniques: Clinical Proteomics; Incubation
bioz_score: 95

title: Headless hemagglutinin-containing influenza viral particles direct immune responses toward more conserved epitopes.
authors: Cait E Hamele; Zhaochen Luo; ...; Nicholas S Heaton
journal: Journal of virology
date: 2024-09-26
pmid: 39324791
doi: 10.1128/jvi.01166-24
cited_by_count: 3
techniques: Activity Assay; Enzyme-linked Immunosorbent Assay; Inhibition; Positive Control
bioz_score: 95

title: Development of a virus-based affinity ultrafiltration method for screening virus-surface-protein-targeted compounds from complex matrixes: Herbal medicines as a case study.
authors: Zhongyuan Li; Baohong Li; ...; Qinghua Cui
journal: Journal of medical virology
date: 2024-03-14
pmid: 38476091
doi: 10.1002/jmv.29517
cited_by_count: 2
techniques: Activity Assay; Binding Assay; Comparison; Concentration Assay; Control; Immunofluorescence; Incubation; Infection; Inhibition; Positive Control; Software; Staining; Virus
bioz_score: 95

title: Compositions and methods for the treatment of viral infections
authors: James M. Balkovec; Daniel C. Bensen; ...; Leslie W. Tari
date: 2023-12-05
cited_by_count: 0
techniques: Concentration Assay; Incubation; Protein Concentration
bioz_score: 92

title: Differential recognition of influenza A virus H1N1 neuraminidase by DNA vaccine-induced antibodies in pigs and ferrets.
authors: Jeanette Linnea Tingstedt; Christine Stephen; ...; Ria Lassaunière
journal: Frontiers in Immunology
date: 2023-06-15
pmid: 37313410
cited_by_count: 1
techniques: Blocking Assay; Enzyme-linked Immunosorbent Assay; Incubation; Serial Dilution
bioz_score: 94

title: Bidirectionally Regulating Viral and Cellular Ferroptosis with Metastable Iron Sulfide Against Influenza Virus
authors: Xinyu Miao; Yinyan Yin; ...; Xiufan Liu
journal: Advanced Science
date: 2023-04-24
pmid: 37092591
pmcid: 10265104
cited_by_count: 14
techniques: Activity Assay; Centrifugation; Expressing; Flow Cytometry; Fluorescence; Immunofluorescence; In Vitro; In Vivo; Incubation; Infection; Inhibition; Marker; Produced; Purification; Quantitative RT-PCR; Software; Staining; Western Blot
bioz_score: 95

title: Antiviral Mechanism of Virucidal Sialic Acid Modified Cyclodextrin
authors: Yong Zhu; Andrey A. Sysoev; ...; Haibing Zhou
journal: Pharmaceutics
date: 2023-02-09
pmid: 36839904
doi: 10.3390/pharmaceutics15020582
pmcid: 9965221
cited_by_count: 20
techniques: Activity Assay; Binding Assay; Concentration Assay; Control; Fluorescence; Incubation; Infection; Inhibition; Labeling; Lysis; Quantitative RT-PCR; Standard Deviation; Two Tailed Test; Virus
bioz_score: 95

title: Enhanced influenza A H1N1 T cell epitope recognition and cross-reactivity to protein-O-mannosyltransferase 1 in Pandemrix-associated narcolepsy type 1
authors: A. Vuorela; T. L. Freitag; ...; O. Vaarala
journal: Nature Communications
date: 2021-04-16
pmid: 33863907
doi: 10.1038/s41467-021-22637-8
pmcid: 8052463
cited_by_count: 26
techniques: Recombinant
bioz_score: 95

title: Methods of detecting influenza virus
authors: Alison A. Weiss; Karen Melissa Gallegos Villalobos; David Ralph
date: 2019-09-10
cited_by_count: 0
techniques: Activity Assay; Concentration Assay; Focus Forming Assay; Purification; Recombinant; Reverse Transcription Polymerase Chain Reaction; Virus
bioz_score: 95

title: Broad-spectrum capture of clinical pathogens using engineered Fc-mannose-binding lectin enhanced by antibiotic treatment
authors: Benjamin T. Seiler; Mark Cartwright; ...; Donald E. Ingber
journal: F1000Research
date: 2019-01-25
pmid: 31275563
doi: 10.12688/f1000research.17447.1
pmcid: 6544136
cited_by_count: 23
techniques: Binding Assay; Laser Capture Microdissection; Purification
bioz_score: 95

title: Inhibition of Influenza A Virus Infection by Fucoidan Targeting Viral Neuraminidase and Cellular EGFR Pathway
authors: Wei Wang; Jiandong Wu; ...; Guangli Yu
journal: Scientific Reports
date: 2017-01-17
pmid: 28094330
doi: 10.1038/srep40760
pmcid: 5240104
cited_by_count: 90
techniques: Activity Assay; Binding Assay; Electron Microscopy; Fluorescence; Incubation; Infection; Labeling; Plasmid Preparation; Recombinant
bioz_score: 95

title: Comparison of reversed-phase liquid chromatography and hydrophilic interaction chromatography for the fingerprint analysis of Radix isatidis.
authors: Cong-En Zhang; Yin Xiong; ...; Dan Yan
journal: Journal of Separation Science
date: 2014-11-14
pmid: 24595986
doi: 10.1002/jssc.201301159
cited_by_count: 2
techniques: Purification
bioz_score: 95

title: Comparison of reversed-phase liquid chromatography and hydrophilic interaction chromatography for the fingerprint analysis ofRadix isatidis
authors: Cong-En Zhang; Yin Xiong; ...; Dan Yan
journal: Journal of Separation Science
date: 2014-04-10
doi: 10.1002/jssc.201301159
cited_by_count: 8
bioz_score: 95

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